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Conserved domains on  [gi|568942376|ref|XP_006506429|]
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rab11 family-interacting protein 5 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C2 super family cl14603
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 21-167 2.54e-47

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


The actual alignment was detected with superfamily member cd08682:

Pssm-ID: 472691 [Multi-domain]  Cd Length: 126  Bit Score: 164.93  E-value: 2.54e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942376   21 VQVTVLRASGLRGKssGAGSTSDAYTVIQVGREKYSTSVVEKTqGCPEWCEECSFELPPGAldgllraqeadagpapwaS 100
Cdd:cd08682     1 VQVTVLQARGLLCK--GKSGTNDAYVIIQLGKEKYSTSVKEKT-TSPVWKEECSFELPGLL------------------S 59

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568942376  101 GPNAACELVLTTMHRSLIGVDKFLGRATVALDEVFRAGRAQHTQWYRLHSKPGKKEKERGEIQVTIQ 167
Cdd:cd08682    60 GNGNRATLQLTVMHRNLLGLDKFLGQVSIPLNDLDEDKGRRRTRWFKLESKPGKDDKERGEIEVDIQ 126
RBD-FIP super family cl09694
FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of ...
 1166-1212 1.78e-07

FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of Rab11-interacting proteins (FIPs). The Rab proteins constitute the largest family of small GTPases (>60 members in mammals). Among them Rab11 is a well characterized regulator of endocytic and recycling pathways. Rab11 associates with a broad range of post-Golgi organelles, including recycling endosomes.


The actual alignment was detected with superfamily member pfam09457:

Pssm-ID: 462805 [Multi-domain]  Cd Length: 41  Bit Score: 48.49  E-value: 1.78e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 568942376  1166 THDELIGLLLQRERELSqrdehvqELESYIDRLLVRIMETSPTLLQI 1212
Cdd:pfam09457    1 SRDELQDALQKQEEENR-------RLEDYIDNILLRIMEHNPSILEV 40
 
Name Accession Description Interval E-value
C2_Rab11-FIP_classI cd08682
C2 domain found in Rab11-family interacting proteins (FIP) class I; Rab GTPases recruit ...
 21-167 2.54e-47

C2 domain found in Rab11-family interacting proteins (FIP) class I; Rab GTPases recruit various effector proteins to organelles and vesicles. Rab11-family interacting proteins (FIPs) are involved in mediating the role of Rab11. FIPs can be divided into three classes: class I FIPs (Rip11a, Rip11b, RCP, and FIP2) which contain a C2 domain after N-terminus of the protein, class II FIPs (FIP3 and FIP4) which contain two EF-hands and a proline rich region, and class III FIPs (FIP1) which exhibits no homology to known protein domains. All FIP proteins contain a highly conserved, 20-amino acid motif at the C-terminus of the protein, known as Rab11/25 binding domain (RBD). Class I FIPs are thought to bind to endocytic membranes via their C2 domain, which interacts directly with phospholipids. Class II FIPs do not have any membrane binding domains leaving much to speculate about the mechanism involving FIP3 and FIP4 interactions with endocytic membranes. The members in this CD are class I FIPs. The exact function of the Rab11 and FIP interaction is unknown, but there is speculation that it involves the role of forming a targeting complex that recruits a group of proteins involved in membrane transport to organelles. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176064 [Multi-domain]  Cd Length: 126  Bit Score: 164.93  E-value: 2.54e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942376   21 VQVTVLRASGLRGKssGAGSTSDAYTVIQVGREKYSTSVVEKTqGCPEWCEECSFELPPGAldgllraqeadagpapwaS 100
Cdd:cd08682     1 VQVTVLQARGLLCK--GKSGTNDAYVIIQLGKEKYSTSVKEKT-TSPVWKEECSFELPGLL------------------S 59

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568942376  101 GPNAACELVLTTMHRSLIGVDKFLGRATVALDEVFRAGRAQHTQWYRLHSKPGKKEKERGEIQVTIQ 167
Cdd:cd08682    60 GNGNRATLQLTVMHRNLLGLDKFLGQVSIPLNDLDEDKGRRRTRWFKLESKPGKDDKERGEIEVDIQ 126
C2 pfam00168
C2 domain;
20-148 7.55e-13

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 65.80  E-value: 7.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942376    20 HVQVTVLRASGLRGKSSGagSTSDAYTVIQV--GREKYSTSVVEKTQgCPEWCEECSFELPPGALDgllraqeadagpap 97
Cdd:pfam00168    2 RLTVTVIEAKNLPPKDGN--GTSDPYVKVYLldGKQKKKTKVVKNTL-NPVWNETFTFSVPDPENA-------------- 64

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568942376    98 wasgpnaacELVLTTMHRSLIGVDKFLGRATVALDEVFRagRAQHTQWYRL 148
Cdd:pfam00168   65 ---------VLEIEVYDYDRFGRDDFIGEVRIPLSELDS--GEGLDGWYPL 104
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 23-142 1.46e-08

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 53.65  E-value: 1.46e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942376     23 VTVLRASGLRGKSSGagSTSDAYTVIQVG---REKYSTSVVEKTqGCPEWCEECSFELPPGALDgllraqeadagpapwa 99
Cdd:smart00239    4 VKIISARNLPPKDKG--GKSDPYVKVSLDgdpKEKKKTKVVKNT-LNPVWNETFEFEVPPPELA---------------- 64

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 568942376    100 sgpnaacELVLTTMHRSLIGVDKFLGRATVALDEVFRAGRAQH 142
Cdd:smart00239   65 -------ELEIEVYDKDRFGRDDFIGQVTIPLSDLLLGGRHEK 100
RBD-FIP pfam09457
FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of ...
 1166-1212 1.78e-07

FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of Rab11-interacting proteins (FIPs). The Rab proteins constitute the largest family of small GTPases (>60 members in mammals). Among them Rab11 is a well characterized regulator of endocytic and recycling pathways. Rab11 associates with a broad range of post-Golgi organelles, including recycling endosomes.


Pssm-ID: 462805 [Multi-domain]  Cd Length: 41  Bit Score: 48.49  E-value: 1.78e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 568942376  1166 THDELIGLLLQRERELSqrdehvqELESYIDRLLVRIMETSPTLLQI 1212
Cdd:pfam09457    1 SRDELQDALQKQEEENR-------RLEDYIDNILLRIMEHNPSILEV 40
 
Name Accession Description Interval E-value
C2_Rab11-FIP_classI cd08682
C2 domain found in Rab11-family interacting proteins (FIP) class I; Rab GTPases recruit ...
 21-167 2.54e-47

C2 domain found in Rab11-family interacting proteins (FIP) class I; Rab GTPases recruit various effector proteins to organelles and vesicles. Rab11-family interacting proteins (FIPs) are involved in mediating the role of Rab11. FIPs can be divided into three classes: class I FIPs (Rip11a, Rip11b, RCP, and FIP2) which contain a C2 domain after N-terminus of the protein, class II FIPs (FIP3 and FIP4) which contain two EF-hands and a proline rich region, and class III FIPs (FIP1) which exhibits no homology to known protein domains. All FIP proteins contain a highly conserved, 20-amino acid motif at the C-terminus of the protein, known as Rab11/25 binding domain (RBD). Class I FIPs are thought to bind to endocytic membranes via their C2 domain, which interacts directly with phospholipids. Class II FIPs do not have any membrane binding domains leaving much to speculate about the mechanism involving FIP3 and FIP4 interactions with endocytic membranes. The members in this CD are class I FIPs. The exact function of the Rab11 and FIP interaction is unknown, but there is speculation that it involves the role of forming a targeting complex that recruits a group of proteins involved in membrane transport to organelles. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176064 [Multi-domain]  Cd Length: 126  Bit Score: 164.93  E-value: 2.54e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942376   21 VQVTVLRASGLRGKssGAGSTSDAYTVIQVGREKYSTSVVEKTqGCPEWCEECSFELPPGAldgllraqeadagpapwaS 100
Cdd:cd08682     1 VQVTVLQARGLLCK--GKSGTNDAYVIIQLGKEKYSTSVKEKT-TSPVWKEECSFELPGLL------------------S 59

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568942376  101 GPNAACELVLTTMHRSLIGVDKFLGRATVALDEVFRAGRAQHTQWYRLHSKPGKKEKERGEIQVTIQ 167
Cdd:cd08682    60 GNGNRATLQLTVMHRNLLGLDKFLGQVSIPLNDLDEDKGRRRTRWFKLESKPGKDDKERGEIEVDIQ 126
C2 pfam00168
C2 domain;
20-148 7.55e-13

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 65.80  E-value: 7.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942376    20 HVQVTVLRASGLRGKSSGagSTSDAYTVIQV--GREKYSTSVVEKTQgCPEWCEECSFELPPGALDgllraqeadagpap 97
Cdd:pfam00168    2 RLTVTVIEAKNLPPKDGN--GTSDPYVKVYLldGKQKKKTKVVKNTL-NPVWNETFTFSVPDPENA-------------- 64

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568942376    98 wasgpnaacELVLTTMHRSLIGVDKFLGRATVALDEVFRagRAQHTQWYRL 148
Cdd:pfam00168   65 ---------VLEIEVYDYDRFGRDDFIGEVRIPLSELDS--GEGLDGWYPL 104
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 21-148 1.90e-12

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 64.78  E-value: 1.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942376   21 VQVTVLRASGLRGKssGAGSTSDAYTVIQVG-REKYSTSVVEKTQgCPEWCEECSFELPPGALDgllraqeadagpapwa 99
Cdd:cd00030     1 LRVTVIEARNLPAK--DLNGKSDPYVKVSLGgKQKFKTKVVKNTL-NPVWNETFEFPVLDPESD---------------- 61

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568942376  100 sgpnaacELVLTTMHRSLIGVDKFLGRATVALDEVFRAGRaQHTQWYRL 148
Cdd:cd00030    62 -------TLTVEVWDKDRFSKDDFLGEVEIPLSELLDSGK-EGELWLPL 102
C2A_Synaptotagmin-like cd04024
C2 domain first repeat present in Synaptotagmin-like proteins; Synaptotagmin is a ...
 23-169 3.41e-11

C2 domain first repeat present in Synaptotagmin-like proteins; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 175990 [Multi-domain]  Cd Length: 128  Bit Score: 62.06  E-value: 3.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942376   23 VTVLRASGLRGKSSGAGSTSDAYTVIQVGREKYSTSVVEKTQGcPEWCEECSFelppgaldgllraqeadagpaPWASGP 102
Cdd:cd04024     5 VHVVEAKDLAAKDRSGKGKSDPYAILSVGAQRFKTQTIPNTLN-PKWNYWCEF---------------------PIFSAQ 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568942376  103 NAACELVLTTMHRSliGVDKFLGRATVALDEVFRAGR-AQHTQWYRLHSK-PGKKEKERGEIQVtiQFT 169
Cdd:cd04024    63 NQLLKLILWDKDRF--AGKDYLGEFDIALEEVFADGKtGQSDKWITLKSTrPGKTSVVSGEIHL--QFS 127
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 23-142 1.46e-08

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 53.65  E-value: 1.46e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942376     23 VTVLRASGLRGKSSGagSTSDAYTVIQVG---REKYSTSVVEKTqGCPEWCEECSFELPPGALDgllraqeadagpapwa 99
Cdd:smart00239    4 VKIISARNLPPKDKG--GKSDPYVKVSLDgdpKEKKKTKVVKNT-LNPVWNETFEFEVPPPELA---------------- 64

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 568942376    100 sgpnaacELVLTTMHRSLIGVDKFLGRATVALDEVFRAGRAQH 142
Cdd:smart00239   65 -------ELEIEVYDKDRFGRDDFIGQVTIPLSDLLLGGRHEK 100
C2B_RasGAP cd08675
C2 domain second repeat of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras ...
 23-162 1.74e-08

C2 domain second repeat of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. The proteins here all contain two tandem C2 domains, a Ras-GAP domain, and a pleckstrin homology (PH)-like domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology.


Pssm-ID: 176057 [Multi-domain]  Cd Length: 137  Bit Score: 54.30  E-value: 1.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942376   23 VTVLRASGLRGKSSGagsTSDAY-TVIQVGREKYS---TSVVEKTQgCPEWCEECSFELPPGALDGLLRAQEADAGPAPw 98
Cdd:cd08675     3 VRVLECRDLALKSNG---TCDPFaRVTLNYSSKTDtkrTKVKKKTN-NPRFDEAFYFELTIGFSYEKKSFKVEEEDLEK- 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568942376   99 asgpnaaCELVLTTMHRSLIGVDKFLGRATVALDEVFRAGraQHTQWYRLH--SKPGKKEKERGEI 162
Cdd:cd08675    78 -------SELRVELWHASMVSGDDFLGEVRIPLQGLQQAG--SHQAWYFLQprEAPGTRSSNDGSL 134
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
 17-154 7.36e-08

C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. There are several classes of Synaptotagmins. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 175975 [Multi-domain]  Cd Length: 134  Bit Score: 52.59  E-value: 7.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942376   17 LPT--HVQVTVLRASGLrgKSSGAGSTSDAY---TVIQVGRE--KYSTSVVEKTQgCPEWCEECSFELPPGALDGllraq 89
Cdd:cd00276    10 LPTaeRLTVVVLKARNL--PPSDGKGLSDPYvkvSLLQGGKKlkKKKTSVKKGTL-NPVFNEAFSFDVPAEQLEE----- 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568942376   90 eadagpapwasgpnaaCELVLTTMHRSLIGVDKFLGRATVALDevfrAGRAQHTQWYRLHSKPGK 154
Cdd:cd00276    82 ----------------VSLVITVVDKDSVGRNEVIGQVVLGPD----SGGEELEHWNEMLASPRK 126
RBD-FIP pfam09457
FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of ...
 1166-1212 1.78e-07

FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of Rab11-interacting proteins (FIPs). The Rab proteins constitute the largest family of small GTPases (>60 members in mammals). Among them Rab11 is a well characterized regulator of endocytic and recycling pathways. Rab11 associates with a broad range of post-Golgi organelles, including recycling endosomes.


Pssm-ID: 462805 [Multi-domain]  Cd Length: 41  Bit Score: 48.49  E-value: 1.78e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 568942376  1166 THDELIGLLLQRERELSqrdehvqELESYIDRLLVRIMETSPTLLQI 1212
Cdd:pfam09457    1 SRDELQDALQKQEEENR-------RLEDYIDNILLRIMEHNPSILEV 40
C2_Munc13_fungal cd04043
C2 domain in Munc13 (mammalian uncoordinated) proteins; fungal group; C2-like domains are ...
 23-132 3.76e-04

C2 domain in Munc13 (mammalian uncoordinated) proteins; fungal group; C2-like domains are thought to be involved in phospholipid binding in a Ca2+ independent manner in both Unc13 and Munc13. Caenorabditis elegans Unc13 has a central domain with sequence similarity to PKC, which includes C1 and C2-related domains. Unc13 binds phorbol esters and DAG with high affinity in a phospholipid manner. Mutations in Unc13 results in abnormal neuronal connections and impairment in cholinergic neurotransmission in the nematode. Munc13 is the mammalian homolog which are expressed in the brain. There are 3 isoforms (Munc13-1, -2, -3) and are thought to play a role in neurotransmitter release and are hypothesized to be high-affinity receptors for phorbol esters. Unc13 and Munc13 contain both C1 and C2 domains. There are two C2 related domains present, one central and one at the carboxyl end. Munc13-1 contains a third C2-like domain. Munc13 interacts with syntaxin, synaptobrevin, and synaptotagmin suggesting a role for these as scaffolding proteins. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-II topology.


Pssm-ID: 176008 [Multi-domain]  Cd Length: 126  Bit Score: 41.48  E-value: 3.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942376   23 VTVLRASGLrgKSSGAGSTSDAYTVI---QVGREKYSTSVVEKTQGcPEWCEEcsFELPpgaldgllraqeadagpapwa 99
Cdd:cd04043     5 IRIVRAENL--KADSSNGLSDPYVTLvdtNGKRRIAKTRTIYDTLN-PRWDEE--FELE--------------------- 58

                          90       100       110
                  ....*....|....*....|....*....|...
gi 568942376  100 SGPNAACELVLTTMHRSLIGVDKFLGRATVALD 132
Cdd:cd04043    59 VPAGEPLWISATVWDRSFVGKHDLCGRASLKLD 91
C2B_RasA1_RasA4 cd04025
C2 domain second repeat present in RasA1 and RasA4; RasA1 and RasA4 are GAP1s (GTPase ...
 24-162 5.37e-04

C2 domain second repeat present in RasA1 and RasA4; RasA1 and RasA4 are GAP1s (GTPase activating protein 1s ), Ras-specific GAP members, which suppresses Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. Both proteins contain two C2 domains, a Ras-GAP domain, a plextrin homology (PH)-like domain, and a Bruton's Tyrosine Kinase (BTK) zinc binding domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 175991 [Multi-domain]  Cd Length: 123  Bit Score: 40.93  E-value: 5.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942376   24 TVLRASGLRGKS-SGagsTSDAYTVIQVGREKYSTSVVEKTQgCPEWCEECSFELPPGAlDGLLRAQEADagpapWasgp 102
Cdd:cd04025     5 HVLEARDLAPKDrNG---TSDPFVRVFYNGQTLETSVVKKSC-YPRWNEVFEFELMEGA-DSPLSVEVWD-----W---- 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942376  103 naacelvlttmhrSLIGVDKFLGRATVALDEVFRAGraQHTQWYRLHSKPGKKEKERGEI 162
Cdd:cd04025    71 -------------DLVSKNDFLGKVVFSIQTLQQAK--QEEGWFRLLPDPRAEEESGGNL 115
C2_Calpain cd04046
C2 domain present in Calpain proteins; A single C2 domain is found in calpains (EC 3.4.22.52, ...
 21-69 7.38e-04

C2 domain present in Calpain proteins; A single C2 domain is found in calpains (EC 3.4.22.52, EC 3.4.22.53), calcium-dependent, non-lysosomal cysteine proteases. Caplains are classified as belonging to Clan CA by MEROPS and include six families: C1, C2, C10, C12, C28, and C47. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176011 [Multi-domain]  Cd Length: 126  Bit Score: 40.72  E-value: 7.38e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568942376   21 VQVTVLRASGLrgKSSGAGSTSDAYTVIQVGREKYSTSVVEKTQGcPEW 69
Cdd:cd04046     5 TQVHVHSAEGL--SKQDSGGGADPYVIIKCEGESVRSPVQKDTLS-PEF 50
C2_SRC2_like cd04051
C2 domain present in Soybean genes Regulated by Cold 2 (SRC2)-like proteins; SRC2 production ...
 21-155 1.94e-03

C2 domain present in Soybean genes Regulated by Cold 2 (SRC2)-like proteins; SRC2 production is a response to pathogen infiltration. The initial response of increased Ca2+ concentrations are coupled to downstream signal transduction pathways via calcium binding proteins. SRC2 contains a single C2 domain which localizes to the plasma membrane and is involved in Ca2+ dependent protein binding. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176016 [Multi-domain]  Cd Length: 125  Bit Score: 39.52  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942376   21 VQVTVLRASGLrgKSSGAGSTSDAYTVIQV-GREKYSTSVVEKTQGCPEWCEECSFELPPGALDGLLRAqeadagpapwa 99
Cdd:cd04051     2 LEITIISAEDL--KNVNLFGKMKVYAVVWIdPSHKQSTPVDRDGGTNPTWNETLRFPLDERLLQQGRLA----------- 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568942376  100 sgpnaaceLVLTTMHRSLIGVDKFLGRATVALDEVFRAGRAQ---HTQWYRLHSKPGKK 155
Cdd:cd04051    69 --------LTIEVYCERPSLGDKLIGEVRVPLKDLLDGASPAgelRFLSYQLRRPSGKP 119
C2B_Munc13 cd04027
C2 domain second repeat in Munc13 (mammalian uncoordinated) proteins; C2-like domains are ...
 21-76 4.63e-03

C2 domain second repeat in Munc13 (mammalian uncoordinated) proteins; C2-like domains are thought to be involved in phospholipid binding in a Ca2+ independent manner in both Unc13 and Munc13. Caenorabditis elegans Unc13 has a central domain with sequence similarity to PKC, which includes C1 and C2-related domains. Unc13 binds phorbol esters and DAG with high affinity in a phospholipid manner. Mutations in Unc13 results in abnormal neuronal connections and impairment in cholinergic neurotransmission in the nematode. Munc13 is the mammalian homolog which are expressed in the brain. There are 3 isoforms (Munc13-1, -2, -3) and are thought to play a role in neurotransmitter release and are hypothesized to be high-affinity receptors for phorbol esters. Unc13 and Munc13 contain both C1 and C2 domains. There are two C2 related domains present, one central and one at the carboxyl end. Munc13-1 contains a third C2-like domain. Munc13 interacts with syntaxin, synaptobrevin, and synaptotagmin suggesting a role for these as scaffolding proteins. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-II topology.


Pssm-ID: 175993 [Multi-domain]  Cd Length: 127  Bit Score: 38.70  E-value: 4.63e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568942376   21 VQVTVLRASGLRGKSSGAgsTSDAYTVIQVGREKYSTSVVEKTQGcPEWCEECSFE 76
Cdd:cd04027     3 ISITVVCAQGLIAKDKTG--TSDPYVTVQVGKTKKRTKTIPQNLN-PVWNEKFHFE 55
C2_putative_Elicitor-responsive_gene cd04049
C2 domain present in the putative elicitor-responsive gene; In plants elicitor-responsive ...
 22-139 6.56e-03

C2 domain present in the putative elicitor-responsive gene; In plants elicitor-responsive proteins are triggered in response to specific elicitor molecules such as glycolproteins, peptides, carbohydrates and lipids. A host of defensive responses are also triggered resulting in localized cell death. Antimicrobial secondary metabolites, such as phytoalexins, or defense-related proteins, including pathogenesis-related (PR) proteins are also produced. There is a single C2 domain present here. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members have a type-II topology.


Pssm-ID: 176014 [Multi-domain]  Cd Length: 124  Bit Score: 38.08  E-value: 6.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942376   22 QVTVLRASGLRGksSGAGSTSDAYTVIQVGREKYSTSVVEKTQGCPEWCEECSFELPPGaldgllraqeadagpapwasG 101
Cdd:cd04049     4 EVLLISAKGLQD--TDFLGKIDPYVIIQCRTQERKSKVAKGDGRNPEWNEKFKFTVEYP--------------------G 61

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568942376  102 PNAACELVLTTMHRSLIGVDKFLGRATVALDEVFRAGR 139
Cdd:cd04049    62 WGGDTKLILRIMDKDNFSDDDFIGEATIHLKGLFEEGV 99
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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